Q88VY1 · PFKA_LACPL
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids320 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic activity
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+
Cofactor
Activity regulation
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 72-73 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RY | ||||||
Binding site | 102-105 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 125-127 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 127 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 162 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 169-171 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 222 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 243 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 249-252 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | monosaccharide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactiplantibacillus
Accessions
- Primary accessionQ88VY1
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000111959 | 1-320 | ATP-dependent 6-phosphofructokinase | |||
Sequence: MKRIGILTSGGDAPGMNAAVRAVAGKAMAEGLEAYGINYGFAGLVAGDIHKIEAADLDGVIQRGGTLLYSARYPEFAHEEGQLKGIEQLKRFGIDALVVIGGDGSYHGALRLTEHGYNTIGLPGTIDNDIPYTDFTIGFDTAVNTNVQALDRIYDTAHSHDRTFVVEVMGRGAGDVALWSGVSIGATAIVVPEVDWDMEEIANKIKHNRANGHRSNLIVLAEGVMGAQEFVEKLSEYGDFDARGNTIAHMQRGGNPTAKDRVMASKMGAYAVELLLAGKGGLAVGIQNNQLVNHNILDLFESKHDVEVSLDKLNEEISFK |
Interaction
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length320
- Mass (Da)34,266
- Last updated2003-06-16 v1
- Checksum8DD32DD469261668
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL935263 EMBL· GenBank· DDBJ | CCC79163.1 EMBL· GenBank· DDBJ | Genomic DNA |